A circular dichroism spectrometer with the capability for rapid reaction kinetics and an associated computer-based work station is requested by faculty in the Chemistry and the Molecular and Cell Biology Departments at Penn State. Drs. Johnson, Lecomte, Matthews, Shamma and Villafranca constitute the major users group for this system. These investigators are involved in a variety of studies many of which focus on the structure, function and folding of proteins. The ability to monitor the ellipticity and thereby, the secondary and tertiary structure of these proteins and peptides is critical in continuing efforts to unravel enzymatic mechanisms, folding mechanisms and the basis for stability in wild type and mutant proteins. Dr. Shamma is interested in the structures of natural products. A brief summary of these research programs follows: Kenneth A. Johnson- Studies on the molecular mechanisms by which chemical and mechanical energy are interconverted during muscle contraction; mechanism of DNA polymeraces and gyrases. Juliette J. T. Lecomte- Structural and dynamic aspects of proteins in solution by nuclear magnetic resonance spectroscopy. C. Robert Matthews- Biophysical studies on the mechanism by which the amino acid sequence of a protein directs the rapid and efficient folding to the native conformation. Maurice Shamma- Isolation, identification and synthesis of natural products, especially isoquinoline alkaloids. Joseph J. Villafranca- Studies on enzyme mechanisms and the structure/function relationships in enzymes.